SASDCV6

Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2021-08-18T17:29:52.846460+02:00

12N12 nucleosomes in the presence of the chromatin remodeler Chd1 in 60% sucrose and ADP-BeF3. The complex formed contains two Chd1 proteins bound to each nucleosome. Due to contrast matching between the solvent and histone proteins, the measured signal is dominated by the DNA component. The models were generated using 3D-DART and custom scripts written in Pymol. The percentage-weighting of each model in the ensemble ('XXXperc') is noted in the following model key/list that sequentially corresponds to models displayed in this entry ordered from top-to-bottom: --------------------------------------------------------------------------------------------------- ---------------SASDCV6_fit1_model1=Chd1_12N12_ADP_01_wrapped_13perc; ---------------SASDCV6_fit1_model2=Chd1_12N12_ADP_02_wrapped_17perc_dyadflip; ---------------SASDCV6_fit1_model3=Chd1_12N12_ADP_03_inplane_20perc_dyadflip; ---------------SASDCV6_fit1_model4=Chd1_12N12_ADP_04_extreme_04perc; ---------------SASDCV6_fit1_model5=Chd1_12N12_ADP_05_extreme_01perc; ---------------SASDCV6_fit1_model6=Chd1_12N12_ADP_06_inplane_02perc; ---------------SASDCV6_fit1_model7=Chd1_12N12_ADP_07_inplane_11perc; ---------------SASDCV6_fit1_model8=Chd1_12N12_ADP_08_inplane_06perc; ---------------SASDCV6_fit1_model9=Chd1_12N12_ADP_09_inplane_03perc; ---------------SASDCV6_fit1_model10=Chd1_12N12_ADP_10_outofplane_01perc; ---------------SASDCV6_fit1_model11=Chd1_12N12_ADP_11_outofplane_08perc_dyadflip; ---------------SASDCV6_fit1_model12=Chd1_12N12_ADP_12_outofplane_04perc; ---------------SASDCV6_fit1_model13=Chd1_12N12_ADP_13_outofplane_10perc_dyadflip.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3

Concentration— – 1.88 Buffer / pH10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2) / 7.8
Experimental temperature25.0 Facility / beamlineCornell High Energy Synchrotron Source (CHESS) / G1
Wavelength0.1109 nmExposure10.0 s × 40

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Chromodomain-helicase-DNA-binding protein 1
View sequence
GPQSTVKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGIDIVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPRFEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIFARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKKDVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASNHPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQMVRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINLMTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAEDHVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQLEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSIGESEVRALYKAILKFGNLKEILDELIADGTLPVKSFEKYGETYDEMMEAAKDCVHEEEKNRKEILEKLEKHATAYRAKLKSGEIKAENQPKDNPLTRLSLKKREKKAVLFNFKGVKSLNAESLLSRVEDLKYLKNLINSNYKDDPLKFSLGNNTPKPVQNWSSNWTKEEDEKLLIGVFKYGYGSWTQIRDDPFLGITDKIFLNEVHNPVAKKSASSSDTTPTPSKKGKGITGSSKKVPGAIHLGRRVDYLLSFLRGGLNTKSPS
proteinSaccharomyces cerevisiaeP32657118–1274dimerMolecule count 2133.115 kDa
169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)
View sequence
CTTTCAGCTGATATCGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATCTTGATATCAGCTGAAAG
DNA———–—monomerMolecule count 152.468 kDa
Histone H2A type 1
View sequence
MSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQSVLLPKKTESAKSAKSK
proteinXenopus laevisP06897—–—monomerMolecule count 113.966 kDa
Histone H2B 1.1
View sequence
MPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
proteinXenopus laevisP02281—–—monomerMolecule count 113.934 kDa
Histone H3.2
View sequence
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
proteinXenopus laevisP842331–136monomerMolecule count 115.388 kDa
Histone H4
View sequence
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
proteinXenopus laevisP62799—–—monomerMolecule count 111.367 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1245[3]0.016–0.26 1/AHas uncertainty columnMissing 012sasbdb/entries/v6/sasdcv6/source/SASDCV6.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)16.5—Å
i0Guinier0.0149830.00026arbitrary
i0P(r)0.01570.00021arbitrary
mwExperimental105.0—kDa
rgGuinier5.310.188Å
rgP(r)5.6620.073Å

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

▼

3. Source Fits and Models Source Fits & Models

Fit 1 · EOM/GAJOE 2.1 r7883

χ²: 0.89CorMap p: 0.4283Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—atomicCustom in-house —100.1—Model Image
2—atomicCustom in-house —100.1—Model Image
3—atomicCustom in-house —100.1—Model Image
4—atomicCustom in-house —100.1—Model Image
5—atomicCustom in-house —100.1—Model Image
6—atomicCustom in-house —100.1—Model Image
7—atomicCustom in-house —100.1—Model Image
8—atomicCustom in-house —100.1—Model Image
9—atomicCustom in-house —100.1—Model Image
10—atomicCustom in-house —100.1—Model Image
11—atomicCustom in-house —100.1—Model Image
12—atomicCustom in-house —100.1—Model Image
13—atomicCustom in-house —100.1—Model Image
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4. Source File Index Source Files

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5. Experiment Description and Publication Experiment & Publication

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6. Complete Source Record Complete Source Record

The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.

Open the original SASBDB entry

Buffer and Sample Properties

Buffer name10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2)Buffer concentration—
pH7.8Additives—
Buffer description60% sucrose ADP-BeF3
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-10-24Storage / measurement temperature25.0 / 25.0
Exposure time10.0Frames40
Wavelength0.1109Sample-to-detector distance2.08
SourceX-ray synchrotronDetectorPilatus 200K
Facility / beamlineCornell High Energy Synchrotron Source (CHESS) / G1 · Ithaca, NY, USA
q range0.16 – 2.6Sample volume / flow rate— / —

Original SASBDB Plots

Experimental I(q)
Experimental I(q)
Experimental I(q), log-log
Experimental I(q), log-log
Guinier plot
Guinier plot
Kratky plot
Kratky plot
P(r) plot
P(r) plot

Downloadable Files

CategoryFileStatusSizeChecksumDownload and View
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pddfsasbdb/entries/v6/sasdcv6/source/SASDCV6.outdownloaded27324bf6c1040d5dc7b35fb66dd7d8c644e52c81ec4630f82d8a4f4524b4b79b5b36bDownloadView source fileSource site
sascifsasbdb/entries/v6/sasdcv6/source/SASDCV6.sascifdownloaded8984d0ce3f46df84221bf8fdc92c0f7d5d9e4d7ba19cdbea345986dc230cb6b0fdc0DownloadView source fileSource site
summarysasbdb/entries/v6/sasdcv6/source/summary.jsondownloaded238246afc54a99f364409e7a043d74eda7a5610c54f0831fd2c429d0aa83d4be6d467DownloadView source fileSource site
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full_entry_zip:source record and ZIP contents (17 items)
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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json:397 field values
Field pathRaw value
codeSASDCV6
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleThe ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome.
project.publication.titleThe ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome.
project.publication.author_listTokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD
project.publication.journalNucleic Acids Res
project.publication.doi10.1093/nar/gky206
project.publication.pmid29850894
project.publication.published_date2018 Jun 1
project.statusreleased
project.submitted_date2017-08-03
project.released_date2018-03-25
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDCV6.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDCV6.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCV6_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCV6_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDCV6_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCV6_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDCV6.sascif
experiment.instrument.detector.typePilatus
experiment.instrument.detector.namePilatus 200K
experiment.instrument.detector.resolution172.0
experiment.instrument.nameCornell High Energy Synchrotron Source (CHESS)
experiment.instrument.cityIthaca, NY
experiment.instrument.countryUSA
experiment.instrument.beamline_nameG1
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
experiment.instrument.line_collimationnull
experiment.instrument.sample_path_lengthnull
experiment.instrument.line_collimation_slitlengthnull
experiment.instrument.line_collimation_integrationwidthnull
experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameChromodomain-helicase-DNA-binding protein 1
experiment.sample.molecule[0].short_nameChd1
experiment.sample.molecule[0].sequenceGPQSTVKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVH EASANPQPEDFHGIDIVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLI KWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLDPYVTAE DIEIMDMERERRLDEFEEFHVPERIIDSQRASLEDGTSQLQYLVKWRRLN YDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPRFEKLS VQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFI SWLIFARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDT IREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEA HRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFLMPGRFT IDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKKDVEKSLPSKTERILR VELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASNHPYLF DNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVL IFSQMVRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDF VFLLSTRAGGLGINLMTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVM VYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNEPNAGEL SAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAEDHVTTPDLGESHLGGE EFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQLEMMN RRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSIGESEV RALYKAILKFGNLKEILDELIADGTLPVKSFEKYGETYDEMMEAAKDCVH EEEKNRKEILEKLEKHATAYRAKLKSGEIKAENQPKDNPLTRLSLKKREK KAVLFNFKGVKSLNAESLLSRVEDLKYLKNLINSNYKDDPLKFSLGNNTP KPVQNWSSNWTKEEDEKLLIGVFKYGYGSWTQIRDDPFLGITDKIFLNEV HNPVAKKSASSSDTTPTPSKKGKGITGSSKKVPGAIHLGRRVDYLLSFLR GGLNTKSPS
experiment.sample.molecule[0].organismSaccharomyces cerevisiae
experiment.sample.molecule[0].uniprot_codeP32657
experiment.sample.molecule[0].uniprot_range_first118
experiment.sample.molecule[0].uniprot_range_last1274
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAAKDISTEVLQNPELYGLRRSHRAAAHQQNYFNDSDDEDDEDNIKQSRRKRMTTIEDDE DEFEDEEGEEDSGEDEDEEDFEEDDDYYGSPIKQNRSKPKSRTKSKSKSKPKSQSEKQST VKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGID IVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLK RLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLED GTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPR FEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIF ARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGK KTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLI TGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKK DVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASN HPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQM VRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINL MTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILE YAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAED HVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQ LEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSIGESEVRALYK AILKFGNLKEILDELIADGTLPVKSFEKYGETYDEMMEAAKDCVHEEEKNRKEILEKLEK HATAYRAKLKSGEIKAENQPKDNPLTRLSLKKREKKAVLFNFKGVKSLNAESLLSRVEDL KYLKNLINSNYKDDPLKFSLGNNTPKPVQNWSSNWTKEEDEKLLIGVFKYGYGSWTQIRD DPFLGITDKIFLNEVHNPVAKKSASSSDTTPTPSKKGKGITGSSKKVPGAIHLGRRVDYL LSFLRGGLNTKSPSADIGSKKLPTGPSKKRQRKPANHSKSMTPEITSSEPANGPPSKRMK ALPKGPAALINNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAHEKEYDSMDEEDCRH TMSAIRTSLKRLRRGGKSLDRKEWAKILKTELTTIGNHIESQKGSSRKASPEKYRKHLWS YSANFWPADVKSTKLMAMYDKITESQKK
experiment.sample.molecule[0].mw133.115
experiment.sample.molecule[0].total_mw266.23
experiment.sample.molecule[0].number_molecules2
experiment.sample.molecule[0].complex_stateTrue
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.molecule[1].long_name169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)
experiment.sample.molecule[1].short_nameDNA
experiment.sample.molecule[1].sequenceCTTTCAGCTGATATCGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATCTTGATATCAGCTGAAAG
experiment.sample.molecule[1].organismnull
experiment.sample.molecule[1].uniprot_codenull
experiment.sample.molecule[1].uniprot_range_firstnull
experiment.sample.molecule[1].uniprot_range_lastnull
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeDNA
experiment.sample.molecule[1].uniprot_sequencenull
experiment.sample.molecule[1].mw52.468
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description12N12 nucleosomes in the presence of the chromatin remodeler Chd1 in 60% sucrose and ADP-BeF3. The complex formed contains two Chd1 proteins bound to each nucleosome. Due to contrast matching between the solvent and histone proteins, the measured signal is dominated by the DNA component. The models were generated using 3D-DART and custom scripts written in Pymol. The percentage-weighting of each model in the ensemble ('XXXperc') is noted in the following model key/list that sequentially corresponds to models displayed in this entry ordered from top-to-bottom: --------------------------------------------------------------------------------------------------- ---------------SASDCV6_fit1_model1=Chd1_12N12_ADP_01_wrapped_13perc; ---------------SASDCV6_fit1_model2=Chd1_12N12_ADP_02_wrapped_17perc_dyadflip; ---------------SASDCV6_fit1_model3=Chd1_12N12_ADP_03_inplane_20perc_dyadflip; ---------------SASDCV6_fit1_model4=Chd1_12N12_ADP_04_extreme_04perc; ---------------SASDCV6_fit1_model5=Chd1_12N12_ADP_05_extreme_01perc; ---------------SASDCV6_fit1_model6=Chd1_12N12_ADP_06_inplane_02perc; ---------------SASDCV6_fit1_model7=Chd1_12N12_ADP_07_inplane_11perc; ---------------SASDCV6_fit1_model8=Chd1_12N12_ADP_08_inplane_06perc; ---------------SASDCV6_fit1_model9=Chd1_12N12_ADP_09_inplane_03perc; ---------------SASDCV6_fit1_model10=Chd1_12N12_ADP_10_outofplane_01perc; ---------------SASDCV6_fit1_model11=Chd1_12N12_ADP_11_outofplane_08perc_dyadflip; ---------------SASDCV6_fit1_model12=Chd1_12N12_ADP_12_outofplane_04perc; ---------------SASDCV6_fit1_model13=Chd1_12N12_ADP_13_outofplane_10perc_dyadflip.
experiment_descriptionSynchrotron SAXS data from solutions of Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3 in 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2), pH 7.8, were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (Ithaca, NY, USA) using a Pilatus Pilatus 200K detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1109 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 1.88 mg/ml was measured at 25°C. 40 successive 10 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted to produce the scattering profile displayed in this entry.
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View the complete summary.json source
{
  "code": "SASDCV6",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome.",
    "publication": {
      "title": "The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome.",
      "author_list": "Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD",
      "journal": "Nucleic Acids Res",
      "doi": "10.1093/nar/gky206",
      "pmid": "29850894",
      "published_date": "2018 Jun 1"
    },
    "status": "released",
    "submitted_date": "2017-08-03",
    "released_date": "2018-03-25"
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  "last_modified": "2021-08-18T17:29:52.846460+02:00",
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}
View the complete manifest.json source
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